A new method of protein structure prediction that incorporates residue–residue co-evolution information into the Rosetta structure prediction program was used to develop models for 58 large protein families that had no previous structural information.
An enrichable cross-linker with optional isotope labeling quadruples the number of cross-linked peptides identified from high-complexity samples, enhancing proteome-wide analysis of protein-protein interactions and protein conformational changes by mass spectrometry.
Synthetic single domain antibody libraries and a binder selection cascade encompassing ribosome and phage display enable the selection of conformation-specific binders against previously intractable membrane proteins within three weeks.
Nramp-family transporters adapt a common fold to a novel mechanism in which the spatial and temporal separation of like-charge transition metal and proton co-substrates circumvents the expected electrostatic repulsion.
Specific and non-specific conformational confinement, via point mutation or cochaperone interaction or macro-molecular crowding, stimulates protein function in Hsp90 by reducing non-productive conformational flexibility.